Biochemical and Mass Spectrometry-Based Approaches to Profile SUMOylation in Human Cells
Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
Standard
Biochemical and Mass Spectrometry-Based Approaches to Profile SUMOylation in Human Cells. / Kessler, Benedikt M; Bursomanno, Sara; McGouran, Joanna F; Hickson, Ian D; Liu, Ying.
Activity-Based Proteomics: Methods and Protocols. ed. / Herman S. Overkleeft; Bogdan I. Florea. Vol. 1491 Humana Press, 2017. p. 131-144 (Methods in Molecular Biology, Vol. 1491).Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - CHAP
T1 - Biochemical and Mass Spectrometry-Based Approaches to Profile SUMOylation in Human Cells
AU - Kessler, Benedikt M
AU - Bursomanno, Sara
AU - McGouran, Joanna F
AU - Hickson, Ian D
AU - Liu, Ying
PY - 2017
Y1 - 2017
N2 - Posttranslational modification of proteins with the small ubiquitin-like modifier (SUMO) regulates protein function in the context of cell cycle and DNA repair. The occurrence of SUMOylation is less frequent as compared to protein modification with ubiquitin, and appears to be controlled by a smaller pool of conjugating and deconjugating enzymes. Mass spectrometry has been instrumental in defining specific as well as proteome-wide views of SUMO-dependent biological processes, and several methodological approaches have been developed in the recent past. Here, we provide an overview of the latest experimental approaches to the study of SUMOylation, and also describe hands-on protocols using a combination of biochemistry and mass spectrometry-based technologies to profile proteins that are SUMOylated in human cells.
AB - Posttranslational modification of proteins with the small ubiquitin-like modifier (SUMO) regulates protein function in the context of cell cycle and DNA repair. The occurrence of SUMOylation is less frequent as compared to protein modification with ubiquitin, and appears to be controlled by a smaller pool of conjugating and deconjugating enzymes. Mass spectrometry has been instrumental in defining specific as well as proteome-wide views of SUMO-dependent biological processes, and several methodological approaches have been developed in the recent past. Here, we provide an overview of the latest experimental approaches to the study of SUMOylation, and also describe hands-on protocols using a combination of biochemistry and mass spectrometry-based technologies to profile proteins that are SUMOylated in human cells.
U2 - 10.1007/978-1-4939-6439-0_10
DO - 10.1007/978-1-4939-6439-0_10
M3 - Book chapter
C2 - 27778286
SN - 978-1-4939-6437-6
VL - 1491
T3 - Methods in Molecular Biology
SP - 131
EP - 144
BT - Activity-Based Proteomics
A2 - Overkleeft, Herman S.
A2 - Florea, Bogdan I.
PB - Humana Press
ER -
ID: 169993150